Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 2 (February 2008)

crystallization communications

Acta Cryst. (2008). F64, 102-104 [ doi:10.1107/S1744309108000341 ]

Crystallization and preliminary crystallographic studies of L30e, a ribosomal protein from Methanocaldococcus jannaschii (MJ1044)

S. Rangarajan, J. Jeyakanthan, P. Mridula, K. Sakamoto, Y. Kitamura, Y. Agari, A. Shinkai, A. Ebihara, S. Kuramitsu, S. Yokoyama and K. Sekar

Abstract: In view of the biological significance of understanding the ribosomal machinery of both prokaryotes and eukaryotes, the L30e ribosomal protein from Methanocaldococcus jannaschii was cloned, overexpressed, purified and crystallized using the microbatch-under-oil method with the crystallization conditions 40% PEG 400, 0.1 M MES pH 6.0 and 5% PEG 3000 at 291 K. A diffraction-quality crystal (0.20 × 0.20 × 0.35 mm) was obtained that belonged to the primitive tetragonal space group P4₃, with unit-cell parameters a = 46.1, b = 46.1, c = 98.5 Å, and diffracted to a resolution of 1.9 Å. Preliminary calculations reveal that the asymmetric unit contains two monomers with a Matthews coefficient (V_M) of 2.16 Å³ Da^-1.

Keywords: ribosomal machinery; thermostability.